6 x 10(-3) RLU cfu(-1). The mutant has a growth pattern and carbofuran degradationability similar to PCL3 wild-type. The luminescent emissionby PCL3:luxAB1 directly correlated with the metabolic activity of the cells. The optimal pH, temperature and n-decanal concentration for luminescence emission are 7.0, 35 degrees C and 0.01%, respectively. PCL3:luxAB1 was used to assess the toxicity of carbofuran and carbofuran phenol in basal salt medium (BSM) in which the different sensitivity of the cells is dependent on the biomass concentration. With the luciferase

system, the degradative fraction of the augmented PCL3:luxAB1 and the difference between the active augmented PCL3:luxAB1 and indigenous microorganisms at the contaminated site could be JQ-EZ-05 price indicated.”
“After the complete

gene of a beta-galactosidase from human isolate Bifidobacterium breve B24 was isolated by PCR and overexpressed in Ipatasertib mouse E. coli, the recombinant beta-galactosidase was purified to homogeneity and characterized for the glycoside transferase (GT) and glycoside hydrolase (GH) activities on lactose. One complete ORF encoding 691 amino acids (2076 bp) was the structural gene, LacA (galA) of the beta-gal gene. The recombinant enzyme shown by activity staining and gel-filtration chromatography was composed of a homodimer of 75 kDa with a total molecular mass of 150 kDa. The Km value for lactose (95.58 mM) was 52.5-fold higher than the corresponding Km values for the synthetic substrate ONPG (1.82 mM). This enzyme with the optimum of pH 7.0 and 45 degrees C could synthesize approximately 42.00% of GOS from 1 M of lactose. About 97.00% of lactose in milk was also quickly hydrolyzed by this enzyme (50 units) at 45 degrees C for 5 h to produce 46.30% of glucose, 46.60% of galactose and 7.10% of GOS. The results suggest that this recombinant beta-galactosidase derived from a human isolate B. breve B24 may be suitable

for both the hydrolysis and synthesis of galacto-oligosaccharides Src inhibitor (GOS) in milk and lactose processing.”
“Although several xylanases have been studied, only few xylanases from marine micro-organisms have been reported. We report here a novel halotolerant xylanase from marine bacterium Bacillus subtilis cho40 isolated from Chorao island of mandovi estuary Goa, India. Extracellular xylanase was produced by using agricultural residue such as wheat bran as carbon source under solid-state fermentation (SSF). The optimal pH and temperature of xylanase were reported to be 6.0 and 60 degrees C, respectively. Xyn40 was highly salt-tolerant, and showed highest activity at 0.5 M NaCl. Xylanase activity was greatly induced (140%) when pre-incubated with 0.5 M NaCl for 4 h. The xylanase gene, xyn40, from marine bacterium B. subtilis cho40 was cloned, and expressed in Escherichia coli. The xylanase gene was 645 bp long and had a 215 amino acid ORF protein with a molecular mass of 22.9 kDa.